› 1ekk

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF HYDROXYETHYLTHIAZOLE KINASE IN THE R3 FORM WITH HYDROXYETHYLTHIAZOLE

Released:
DOI: 10.2210/pdb1ekk/pdb
PDB entry 1ekk coloured by chain, front view.
PDB entry 1ekk coloured by chain, side view.
PDB entry 1ekk coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Crystal structure of 4-methyl-5-beta-hydroxyethylthiazole kinase from Bacillus subtilis at 1.5 A resolution.
Campobasso N, Mathews II, Begley TP, Ealick SE
Biochemistry 39 7868-77 (2000)
PMID: 10891066

Function and Biology Details

Reaction catalysed: 
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo trimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153900 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydroxyethylthiazole kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 272 amino acids
Theoretical weight: 28.27 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P39593 (Residues: 1-272; Coverage: 100%)
Gene names: BSU38300, ipa-25d, thiK, thiM, ywbJ
Sequence domains: Hydroxyethylthiazole kinase family
Structure domains: UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase

Ligands and Environments

2 bound ligands:
Ligand TZE 2 x TZE
Ligand SO2 2 x SO2
1 modified residue:
Ligand CSD 2 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: R3
Unit cell:
a: 78.04Å b: 78.04Å c: 232.84Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.205 0.242
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The structural and biochemical foundations of thiamin biosynthesis.
Jurgenson et al. (2009)
2 more

3 mentions without citation

Functional analysis of the glycero-manno-heptose 7-phosphate kinase domain from the bifunctional HldE protein, which is involved in ADP-L-glycero-D-manno-heptose biosynthesis.
McArthur et al. (2005)
2 more